α-Parvin (D7F9) XP? Rabbit mAb

• 产品编号：CST-8190S      品牌：CST       原厂货号：8190S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

α-Parvin (D7F9) XP®兔源单抗识别内源性总α-Parvin 蛋白。单抗由合成肽段免疫动物产生，该合成肽段对应人α-parvin蛋白的N氨基末端附近残基。细胞外基质(ECM)是围绕在哺乳动物器官和组织周围的分泌性大分子复合物结构。在细胞和ECM间受控制的相互作用在增殖和迁移，存活，极化和分化中很重要。细胞最初通过异种二聚化的结合膜蛋白质类整合素来接触ECM， 整合素通过叫做连接ECM到细胞骨架，再到细胞信号机制（1）。ILK/PINCH/Parvin (IPP)复合物由三个高度保守蛋白组成，蛋白被招募到ECM接触的位点，作为前组装结构。IPP在整合素/肌动蛋白连接处表面起作用，调控焦点粘着的形成和整合素信号。所有三种蛋白含多蛋白结合结构域，使得它们在焦点粘着形成中能作为衔接蛋白起功能。ILK（整合素连接激酶）也有一个催化（蛋白丝氨酸/苏氨酸激酶）结构域，并可能也可能不作为激酶起功能在体内。IPP蛋白的作用在IPP复合物外已有研究，包括基基因表达调控（2,3）。Parvin家族有3成员：α-parvin/actopaxin, β-parvin/affixin, 和γ-parvin组成。α-parvin 和β-parvin广泛表达，但γ-parvin表达只限于造血细胞（4）。α-parvin直接结合f-actin并通过与焦点粘着蛋白paxillin相互作用（5）。α-parvin通过与cofilin 激酶TESK1（6）和GTP酶激活蛋白CdGAP（7）相互作用调控细胞的扩散和迁移，在有丝分裂中α-parvin磷酸化可能在细胞周期actin动力学调控中起作用（8）。

1. Burridge, K. et al. (1988) Annu Rev Cell Biol 4, 487-525.
2. Legate, K.R. et al. (2006) Nat Rev Mol Cell Biol 7, 20-31.
3. Wu, C. (2004) Biochim Biophys Acta 1692, 55-62.
4. Korenbaum, E. et al. (2001) Gene 279, 69-79.
5. Nikolopoulos, S.N. and Turner, C.E. (2000) J Cell Biol 151, 1435-48.
6. LaLonde, D.P. et al. (2005) J Biol Chem 280, 21680-8.
7. LaLonde, D.P. et al. (2006) Curr Biol 16, 1375-85.
8. Curtis, M. et al. (2002) Biochem J 363, 233-42.

原厂资料：

Specificity / Sensitivity

α-Parvin (D7F9) XP® Rabbit mAb recognizes endogenous levels of total α-parvin protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human α-parvin protein.

Background

The extracellular matrix (ECM) is a complex structure of secreted macromolecules surrounding mammalian organs and tissues. Controlled interactions between cells and the ECM are important in proliferation, migration, survival, polarity, and differentiation. Cells contact the ECM primarily through heterodimeric integral membrane proteins called integrins. Integrins connect the ECM to the cytoskeleton, and therefore the cell signaling machinery, through protein complexes called focal adhesions (1). 
 The ILK/PINCH/Parvin (IPP) complex is composed of three highly conserved proteins recruited to sites of ECM contact as pre-assembled structures. The IPP acts at the interface of the integrin/actin connection to regulate formation of focal adhesions and integrin signaling. All three proteins contain multiple protein binding domains allowing them to function as adaptor proteins in the formation of focal adhesions. ILK (integrin-linked kinase) also has a catalytic (protein Ser/Thr kinase) domain, and may or may not function as a kinase in vivo. Roles for IPP proteins outside of the IPP complex have been proposed, including regulation of gene expression (2,3). 
 The parvin family consists of 3 members, α-parvin/actopaxin, β-parvin/affixin, and γ-parvin. α-parvin and β-parvin are expressed ubiquitously, while expression of γ-parvin is restricted to hematopoietic cells (4). α-parvin binds to f-actin both directly and via interaction with the focal adhesion protein paxillin (5). α-parvin regulates cell spreading and motility through interactions with the cofilin kinase TESK1 (6), and with the GTPase activating protein CdGAP (7). Phosphorylation of α-parvin during mitosis may have a role in the regulation of actin dynamics during the cell cycle (8).

1. Burridge, K. et al. (1988) Annu Rev Cell Biol 4, 487-525.
2. Legate, K.R. et al. (2006) Nat Rev Mol Cell Biol 7, 20-31.
3. Wu, C. (2004) Biochim Biophys Acta 1692, 55-62.
4. Korenbaum, E. et al. (2001) Gene 279, 69-79.
5. Nikolopoulos, S.N. and Turner, C.E. (2000) J Cell Biol 151, 1435-48.
6. LaLonde, D.P. et al. (2005) J Biol Chem 280, 21680-8.
7. LaLonde, D.P. et al. (2006) Curr Biol 16, 1375-85.
8. Curtis, M. et al. (2002) Biochem J 363, 233-42.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150
mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02%
sodium azide. Store at –20°C. Do not aliquot the antibody.